Ryosuke Tomiyama, Masatomo So, Yohei Miyanoiri, Kazumasa Sakurai. The Residual Structure of Acid-Denatured Β2-Microglobulin is Relevant to an Ordered Fibril Morphology. SSRN Electronic Journal. 2022. 32. 1
Kazumasa Sakurai, Ryosuke Tomiyama. Enhanced accessibility and hydrophobicity of amyloidogenic intermediates of the β2-microglobulin D76N mutant revealed by high-pressure experiments. Journal of Biological Chemistry. 2021. 296. 100333-100333
Koki Furukawa, Cesar Aguirre, Masatomo So, Kenji Sasahara, Yohei Miyanoiri, Kazumasa Sakurai, Keiichi Yamaguchi, Kensuke Ikenaka, Hideki Mochizuki, Jozsef Kardos, et al. Isoelectric point-amyloid formation of α-synuclein extends the generality of the solubility and supersaturation-limited mechanism. Current Research in Structural Biology. 2020. 2. 35-44
Noji M, Sasahara K, Yamaguchi K, So M, Sakurai K, Kardos J, Naiki H, Goto Y. Heating during agitation of β2-microglobulin reveals that supersaturation breakdown is required for amyloid fibril formation at neutral pH. The Journal of biological chemistry. 2019. in press. 43. 15826-15835
Detection method for inter-residue concerted conformational change in a protein molecule by analyzing perturbation-induced multi-dimensional chemical shift changes
(the 30th International Conference on Magnetic Resonance in Biological Systems 2024)
Study on the Inhibitory Effect of Plant Leaf Extracts on Amyloid Fibril Formation of β2-Microglobulin
(The Annual Plant Biology Meeting 2024)
